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Database: UniProt
Entry: R7SWE9_DICSQ
LinkDB: R7SWE9_DICSQ
Original site: R7SWE9_DICSQ 
ID   R7SWE9_DICSQ            Unreviewed;       416 AA.
AC   R7SWE9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   08-NOV-2023, entry version 56.
DE   SubName: Full=Protease {ECO:0000313|EMBL:EJF60406.1};
GN   ORFNames=DICSQDRAFT_127694 {ECO:0000313|EMBL:EJF60406.1};
OS   Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Dichomitus.
OX   NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF60406.1, ECO:0000313|Proteomes:UP000053319};
RN   [1] {ECO:0000313|EMBL:EJF60406.1, ECO:0000313|Proteomes:UP000053319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF60406.1,
RC   ECO:0000313|Proteomes:UP000053319};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; JH719416; EJF60406.1; -; Genomic_DNA.
DR   RefSeq; XP_007366824.1; XM_007366762.1.
DR   AlphaFoldDB; R7SWE9; -.
DR   GeneID; 18834405; -.
DR   KEGG; dsq:DICSQDRAFT_127694; -.
DR   HOGENOM; CLU_013253_1_4_1; -.
DR   OMA; SCIANGW; -.
DR   OrthoDB; 1537596at2759; -.
DR   Proteomes; UP000053319; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EJF60406.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053319};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..416
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004445055"
FT   DOMAIN          109..413
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          142..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        302
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        339..373
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   416 AA;  43710 MW;  5B560E0D84D8D3D7 CRC64;
     MFCKAALITV ALALIASASP IVKPSSGIRI PIQKRGSLTN EDGTFNAEKV ARELVRVQNK
     HRQNLINLKN NVGVKAFNKG ASIKPLATIP THVKRDGVDL TDQENDLLWT GEITIGTDDQ
     KFVIDFDTGS SDLWVPSTSC DSCGSHNKYD PSTSGKKESG SFSISYGDGS TASGDPYTDT
     VTVGGVKVNG QYLAAVTQES SEFQSDPSDG LLGLAFPAIS SLNHDPFFFT AVSQGTAKEG
     RFGFKLASSG SELYIGGTNS DLYKGDIEYH DISSDNGFWQ IGGASVSVGG KSVADSFDTI
     IDSGSTIITA PTDAAKSFWD AVDGSDVYDS SQGLYSYPCD SAPEVSFNWG GKDWAISSEN
     LSLGETESGS GSCVGAISGG DLGLGDNVWL LGDTLLKNTY TVFSVDDNGV GFAELA
//
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